title: Ethylenediaminetetraacetic acid (disodium salt)-labile bovine immunoglobulin M Fc binding to Brucella abortus: a cause of nonspecific agglutination.
abstract: It was demonstrated by a radioimmunoassay procedure that Brucella abortus agglutinins from noninfected cattle sera, absorbed to B. abortus antigen and eluted with ethylenediaminetetraacetic acid (EDTA), was immunoglobulin M that bound to that bacterium by its Fc portion. The EDTA-eluted immunoglobulin M agglutinated intact B. abortus cells but not erythrocytes treated with B. abortus lipopolysaccharide. The specificity of the EDTA-eluted immunoglobulin was for B. abortus, although a small titer to Yersinia enterocolitica serotype O:9 was observed. In contrast, immunoglobulin M purified from the serum of a cow injected 7 days previously with heat-killed B. abortus bound to the antigen by its Fab portion, was not labile to EDTA treatment, cross-reacted extensively with Y. enterocolitica serotype O:9, and agglutinated various other bacterial antigens and normal erythrocytes.
mesh_terms: D000818:Animals; D000937:Antigen-Antibody Reactions; D002003:Brucella abortus / Q000276:immunology*; D002007:Brucellosis, Bovine / Q000175:diagnosis*; D002417:Cattle; D004492:Edetic Acid / Q000494:pharmacology*; D005260:Female; D006386:Hemagglutination Tests / Q000662:veterinary*; D007141:Immunoglobulin Fc Fragments / Q000276:immunology*; D007075:Immunoglobulin M / Q000276:immunology*; D010206:Papain / Q000494:pharmacology
chemical_list: D007141:Immunoglobulin Fc Fragments; D007075:Immunoglobulin M; D004492:Edetic Acid; D010206:Papain